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KMID : 1094720100150060984
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Biotechnology and Bioprocess Engineering
2010 Volume.15 No. 6 p.984 ~ p.992
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Statistical optimization of Bacillus alcalophilus α-amylase immobilization on iron-oxide magnetic nanoparticles
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Mukherjee Ashis K.
Kumar Tadi Satish
Rai Sudhir K.
Roy Jetendra K.
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Abstract
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We report the statistical optimization of the immobilization of alkaline α-amylase [E.C. 3.2.1.1] from Bacillus alcalophilus onto nano-sized supermagnetic ironoxide nanoparticles (MNPs) for augmenting the cost effective industrial application of MNP-bound α-amylase. Both Plackett-Burman factorial design and response surface methodology (RSM) were employed to screen the influence of different parameters and the central effect of response on the α-amylase-iron oxide MNP binding process. The high coefficient of determination (R2) and analysis of variance (ANOVA) of the quadratic model indicated the competence of the proposed model. The size of the MNPs was confirmed by X-ray diffraction and scanning electron microscope analyses in which Fourier transform infrared spectroscopy suggested immobilization of the enzyme on iron-oxide MNPs. A significant improvement (∼ 26-fold) in specific activity, thermal and storage stability, and reusability of α-amylase after binding with iron-oxide MNP reinforced the improved biotechnological potential of the α-amylase iron-oxide MNP bioconjugate compared to free α-amylase. These results open new avenues for applying this MNP immobilized enzyme in different industrial sectors, notably in the paper and brewing industries.
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KEYWORD
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alkaline α-amylase, Bacillus alcalophilus, magnetic nanoparticles, Plackett-Burman design, response surface, starch hydrolysis
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